[Isolation and characterization of the lytic enzyme from Bacillus subtilis 797].
The isolation procedure and some properties of the lytic enzyme produced by Bacillus subtilis 797 and capable of hydrolyzing the E. coli K-12 cells are described. Using hydrophobic chromatography on DNP-hexamethylene diamine Sepharose 4B and ion-exchange chromatography on DEAE-cellulose, a highly purified enzyme preparation with mol. weight of 28000, pI 8.2 has been obtained. The amino acid composition of the enzyme has been determined: Asp--37, Thr--17, Ser--34, Glu--15, Pro--14, Gly--17, Ala--36, Val--28, Met--4, Ile--11, Leu--17, Tyr--9, Phe--4, Lys--18, His--5, Arg--4. The enzyme is inhibited by a specific inhibitor of serine proteinases--benzylsulfonylfluoride, and is insensitive to EDTA and iodoacetic acid. The lytic enzyme has a proteolytic activity and splits the peptide substrate of bacterial serine proteinases--p-nitroanilide benzyloxycarbonyl-L-analyl-L-alanyl-L-leucine; the maxima for both activities lie within the pH range of 7.8-8.5. The lytic protease has the highest stability at pH 6-10. In some of its properties the enzyme is similar to serine proteinase from Bac. subtilis, i. e. subtilisins.
D000596:Amino Acids / Q000032:analysis; D001412:Bacillus subtilis / Q000201:enzymology*; D001433:Bacteriolysis; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity; D013381:Subtilisins / Q000378:metabolism
D000596:Amino Acids; D010447:Peptide Hydrolases; D013381:Subtilisins
Vydelenie i kharakteristika liticheskogo fermenta iz Bacillus subtilis 979.